ID Q1Z608_9GAMM Unreviewed; 300 AA.
AC Q1Z608;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 03-MAY-2023, entry version 41.
DE RecName: Full=Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase {ECO:0000256|PIRNR:PIRNR011468};
DE Short=PRPn C-P lyase {ECO:0000256|PIRNR:PIRNR011468};
DE EC=4.7.1.1 {ECO:0000256|PIRNR:PIRNR011468};
GN ORFNames=P3TCK_12646 {ECO:0000313|EMBL:EAS44036.1};
OS Photobacterium profundum 3TCK.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS44036.1, ECO:0000313|Proteomes:UP000003789};
RN [1] {ECO:0000313|EMBL:EAS44036.1, ECO:0000313|Proteomes:UP000003789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3TCK {ECO:0000313|EMBL:EAS44036.1,
RC ECO:0000313|Proteomes:UP000003789};
RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the breakage of the C-P bond in alpha-D-ribose 1-
CC methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose.
CC {ECO:0000256|PIRNR:PIRNR011468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + alpha-D-ribose 1-methylphosphonate 5-phosphate + S-
CC adenosyl-L-methionine = 5'-deoxyadenosine + A + alpha-D-ribose 1,2-
CC cyclic phosphate 5-phosphate + H(+) + L-methionine + methane;
CC Xref=Rhea:RHEA:34707, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16183, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:68686,
CC ChEBI:CHEBI:68687; EC=4.7.1.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR011468};
CC -!- SIMILARITY: Belongs to the PhnJ family.
CC {ECO:0000256|PIRNR:PIRNR011468}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAS44036.1}.
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DR EMBL; AAPH01000007; EAS44036.1; -; Genomic_DNA.
DR RefSeq; WP_006230551.1; NZ_CH724134.1.
DR AlphaFoldDB; Q1Z608; -.
DR HOGENOM; CLU_063386_0_0_6; -.
DR OrthoDB; 9803851at2; -.
DR Proteomes; UP000003789; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0098848; F:alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019700; P:organic phosphonate catabolic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR010306; PhnJ.
DR Pfam; PF06007; PhnJ; 1.
DR PIRSF; PIRSF011468; PhnJ; 1.
DR SFLD; SFLDF00379; Phosphonate_metabolism_(PhnJ); 1.
DR SFLD; SFLDG01115; Phosphonate_metabolism_(PhnJ); 1.
DR SFLD; SFLDS00033; Radical_SAM_Phosphonate_Metabo; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR011468};
KW Iron {ECO:0000256|PIRNR:PIRNR011468};
KW Iron-sulfur {ECO:0000256|PIRNR:PIRNR011468};
KW Lyase {ECO:0000256|PIRNR:PIRNR011468};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR011468};
KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR011468}.
SQ SEQUENCE 300 AA; 33852 MW; D764D1C7284935DE CRC64;
MSQVINASST CQSDDSNTDS CTDYNTGYNY GYLDEQTKRM IRRSLLKAVA IPGYQVPFGG
REMPMPYGWG TGGVQLTAAI LGQADTLKVI DQGADDTTNA VSIREFFKTV ADARTTERTV
DATVIQTRHR IPEVLLKKDQ ILVYQVPIPE PLRFIEPRET ETRKMHALQE YGIMHVKLYE
DIARFGHIAT AYAYPVRVND RYIMDPSPIP KFDNPKMDNM PALQLFGAGR EKRIYAIPPF
TKVRSLDFED HPFEIQQWDE PCSICGATNT FLDEVVTDDE GNRMFVCSDT DYCGSQGESA
//
